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Study Guide Chapter 16 Solved

The study guide covers the properties of glycine at different pH levels, including its structural formulas and overall charges. It also discusses various protein structures and the effects of pH on enzyme activity, specifically urease, as well as types of enzyme inhibition, including competitive and non-competitive inhibition. Key examples include the irreversible inhibition caused by Sarin on acetylcholinesterase.

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2 views2 pages

Study Guide Chapter 16 Solved

The study guide covers the properties of glycine at different pH levels, including its structural formulas and overall charges. It also discusses various protein structures and the effects of pH on enzyme activity, specifically urease, as well as types of enzyme inhibition, including competitive and non-competitive inhibition. Key examples include the irreversible inhibition caused by Sarin on acetylcholinesterase.

Uploaded by

hookcrystal19
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as DOCX, PDF, TXT or read online on Scribd

Study Guide Ch 16

1. The pI of glycine is 6.0. Draw the condensed structural formulas for glycine
at a. pH 6.0 and at b. pH 8.0. State the overall charge for each.

2. Draw the condensed structural formula for glycine at pH 3.0 and give the
overall charge.

3. Indicate whether the following conditions are responsible for primary,


secondary, tertiary, or quaternary protein structures:
a. disulfide bonds that form between portions of a protein chain
Tertiary structure
b. peptide bonds that form a chain of amino acids
Primary structure
c. hydrogen bonds between the H of a peptide bond and the O of a peptide
bond four amino acids away
Secondary structure

4. If the enzyme urease has an optimum pH of 7.0, what is the effect of


lowering the pH to 3?
If the enzyme urease has an optimum pH of 7.0, lowering the pH to 3 will
significantly denature the enzyme.
5. What type of inhibition occurs when Sarin, a nerve gas, forms a covalent
bond with the R group of serine in the active site of acetylcholinesterase?
When Sarin, a nerve gas, forms a covalent bond with the R group of serine
in the active site of acetylcholinesterase, it results in irreversible inhibition
of the enzyme.
6. State the type of inhibition in the following:
a. The inhibitor has a structure that is similar to the substrate.
Competitive inhibition
b. This inhibitor binds to the surface of the enzyme, changing its shape in such
a way that it cannot bind to substrate.
Non - competitive inhibition

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